ID G8TD59_NIAKG Unreviewed; 482 AA.
AC G8TD59;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=WD40 repeat-containing protein {ECO:0000313|EMBL:AEV98291.1};
GN OrderedLocusNames=Niako_1935 {ECO:0000313|EMBL:AEV98291.1};
OS Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS GR20-10).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV98291.1, ECO:0000313|Proteomes:UP000005438};
RN [1] {ECO:0000313|EMBL:AEV98291.1, ECO:0000313|Proteomes:UP000005438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC {ECO:0000313|Proteomes:UP000005438};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Niastella koreensis GR20-10.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003178; AEV98291.1; -; Genomic_DNA.
DR RefSeq; WP_014218205.1; NC_016609.1.
DR AlphaFoldDB; G8TD59; -.
DR STRING; 700598.Niako_1935; -.
DR KEGG; nko:Niako_1935; -.
DR PATRIC; fig|700598.3.peg.1978; -.
DR eggNOG; COG2319; Bacteria.
DR HOGENOM; CLU_540651_0_0_10; -.
DR Proteomes; UP000005438; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR PANTHER; PTHR44129:SF13; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 16..199
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
FT REPEAT 212..252
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 331..371
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 412..444
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 450..482
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 482 AA; 54414 MW; 9EF444BDF9D6F658 CRC64;
MATRLSVQHV LPDSNFTCFV IPSLFSQTAC EALLNTEIKN SFQKANSNYP TYYRNNDRFV
IDDEALAARL FQKVKPYLPT TIEVNNAIPA ENGTWQLKEL NTRLRFCKYS ANQYFHRHLD
GVHYRSETVQ SKLTFMIYLN SATEFKGGRT LFFKTKETNE IWASYIPKQG DLIVFDHNVW
HEGEVLSEGE KFVLRSDILY SRTNGSSQKE PFAGHLGYIW SLLKFDDDTI LSGGRDTSIK
AWSIAGEEKM SLKEHRNSIL SLAKINANTF ISGSRDQHII VWKDFKAIQK IRIHNALVLS
LCRITDNTFA SGSGDNTIHL ADLNGTILQT FTGHTNWVWQ VLQLNEQTIA SASEDQSIKI
WNKATGQQLA SFTENAPVIS LAFHAPTNQL ISGNLHGDIT IRTLNNNSST TFKAHNGIIR
TIKVINNTLA TGGEDNKVKL WDFNGQLLTG LEHQNFVQSI EQLADNAIIS ASYDGTIRVW
EI
//
